Characterization of novel endo-β-N-acetylglucosaminidase from Bacteroides nordii that hydrolyzes multi-branched complex type N-glycans

Kristina Mae Bienes, Feunai Agape Papalii Tautau, Ai Mitani, Takashi Kinoshita, Shin ichi Nakakita, Yujiro Higuchi, Kaoru Takegawa

Research output: Contribution to journalArticlepeer-review

3 Citations (Scopus)

Abstract

Endo-β-N-acetylglucosaminidases (ENGases) are enzymes that hydrolyze the N-linked oligosaccharides. Many ENGases have already been identified and characterized. However, there are still a few enzymes that have hydrolytic activity toward multibranched complex-type N-glycans on glycoproteins. In this study, one novel ENGase from Bacteroides nordii (Endo-BN) species was identified and characterized. The recombinant protein was prepared and expressed in Escherichia coli cells. This Endo-BN exhibited optimum hydrolytic activity at pH 4.0. High performance liquid chromatography (HPLC) analysis showed that Endo-BN preferred core-fucosylated complex-type N-glycans, with galactose or α2,6-linked sialic acid residues at their non-reducing ends. The hydrolytic activities of Endo-BN were also tested on different glycoproteins from high-mannose type to complex-type oligosaccharides. The reaction with human transferrin, fetuin, and α1-acid glycoprotein subsequently showed that Endo-BN is capable of releasing multi-branched complex-type N-glycans from these glycoproteins.

Original languageEnglish
Pages (from-to)7-13
Number of pages7
JournalJournal of Bioscience and Bioengineering
Volume134
Issue number1
DOIs
Publication statusPublished - Jul 2022

All Science Journal Classification (ASJC) codes

  • Biotechnology
  • Bioengineering
  • Applied Microbiology and Biotechnology

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